video record
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Description
This is the second of two programmes on the structure and action of lysozyme. The programme describes the action of lysozyme on bacterial cell walls.
Metadata describing this Open University video programme
Module code and title: S322, Biochemistry and molecular biology
Item code: S322; 04
Recording date: 20-05-1976
First transmission date: 1977
Published: 1977
Rights Statement:
Restrictions on use:
Duration: 00:23:38
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Producer: Jack Koumi
Contributor: David Phillips
Publisher: BBC Open University
Keyword(s): `Cleft'; Bacterial cell walls; Computer animations; Lysozyme structure; Microscopy; Model
Footage description: The programme starts by summarising TV.3 "The Structure of Lysozyme" with a sequence in which various rotating models of the lysozyme molecule are superimposed to highlight some distinctive features, ending with the "cleft" which is involved in the action. Professor David Phillips of Oxford University explains that to describe the action of lysozyme, it is relevant to consider why the chain molecule takes up its particular globular shape. The model used in TV3, of the chain of 129 amino-acid residues, changes colour to distinguish between the hydrophilic and hydrophobic side-chains. A computer animated film builds up the molecule to show that hydrophilic side-chains remain on the surface, whereas hydrophobic side-chains are folded into the interior. This is illustrated again on a "hydrophilic/hydrophobic" model of the molecule. The action of lysozyme on bacterial cell walls is described using a microscopy film, three video animation sequences describing the polysaccharide structure of a cell wall, a model of the active site attached to a six-ring segment of a polysaccharide, two separate models of this hexasaccharide, an animated film of the action and, finally, the earlier "hydrophilic/hydrophobic" model of lysozyme. The programme ends with various superimpositions of the rotating globular-shaped models.
Master spool number: 6HT/72224
Production number: 00525_1261
Videofinder number: 1010
Available to public: no